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Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin
Author(s) -
Aneja Babita,
Kumari Meena,
Azam Amir,
Kumar Amit,
Abid Mohammad,
Patel Rajan
Publication year - 2018
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3435
Subject(s) - bovine serum albumin , circular dichroism , tryptophan , chemistry , in silico , fluorescence , quenching (fluorescence) , hydrophobic effect , fluorophore , stereochemistry , biochemistry , amino acid , physics , quantum mechanics , gene
The effect of a potent antimicrobial compound bearing 1,2,3‐triazole core and a tryptophan tail, triazole‐tryptophan hybrid (TTH), with bovine serum albumin (BSA) have been explored using various spectroscopic and molecular docking methods. Studies revealed that TTH strongly quenches the intrinsic fluorophore of BSA by a static quenching mechanism. Time‐resolved fluorescence spectra further confirmed the involvement of static quenching for TTH–BSA system. The calculated thermodynamic parameters; Δ H , Δ S , and Δ G showed that the binding process was spontaneous, exothermic and entropy driven. Synchronous fluorescence, three‐dimensional (3D) fluorescence and circular dichroism data revealed that TTH induces the structural alteration in BSA and enhances its stability. In silico study of TTH–BSA system showed that it binds with BSA at the site I of subdomain IIA. Both the experimental and in silico study showed that the hydrophobic and electrostatic interactions play a major role in TTH–BSA binding.